Assistant Professor of Biology
Ph.D. Mount Sinai School of Medicine, 1998
Areas of interest: Molecular and cellular basis of synaptic function in neurodevelopment and neurodegenerative disease
Brain function requires proper networking and communication between neurons. Brain development is a complex process that involves the movement and proper connectivity of neurons. Mutations in certain genes lead to improper neuron movement and brain development that often lead to severe learning disabilities in children. We are studying a specific pathway that controls one aspect of neuron movement and brain development. A better understanding of the molecular mechanism of how genes affect neuronal migration and development will eventually lead to advances in diagnosis and treatment.
Alzheimer’s disease (AD) is a devastating age-associated neurodegenerative disorder characterized by progressive memory loss and cognitive decline. AD affects millions of people world-wide and the disease is becoming more prevalent as the population ages marking as a major public health concern. The main neuropathological hallmark of AD is amyloid plaques that consist of aggregated amyloid peptides derived from the proteolytic cleavage of the amyloid precursor protein (APP). Understanding the cell biology and molecules controlling APP localization and processing is of great significance for the mechanistic understanding of AD. It will provide novel insights into AD pathogenesis and can lead to the development of novel therapeutic strategies for treating or preventing AD.
- BI 325 Principles of Neurobiology
- BI481 Molecular Biology of the Neuron
- BI582 Seminar in Biology - Neurodegeneration
- Sullivan SE, Dillon GM, Sullivan JM, Ho A (2014) Mint proteins are required for synaptic activity-dependent APP trafficking and amyloid-beta generation. Journal of Biological Chemistry, 289:15374-15383.
- Beffert U, Dillon GM, Sullivan JM, Stuart CE, Gilbert JP, Kambouris JA, Ho A (2012) Microtubule plus-end tracking protein CLASP2 regulates neuronal polarity and synaptic function. Journal of Neuroscience, 32: 13906-13916.
- Chaufty J, Sullivan SE, Ho A (2012) Intracellular APP sorting and Aß secretion are regulated by src-mediated phosphorylation of Mint2. Journal of Neuroscience, 32: 9613-9625.
- Matos MF, Xu Y, Dulubova I, Otwinowski Z, Richardson III JM, Tomchick DR, Rizo J, Ho A (2012) Autoinhibition of Mint1 adaptor protein regulates APP binding and processing. Proceedings National Academy Sciences USA 109: 3802-3807.
- Ho A and Shen J (2011) Presenilins in synaptic function and disease. Trends in Molecular Medicine 17: 617-624.
- Ho A, Liu X, Südhof TC (2008) Deletion of mint proteins decreases amyloid production in transgenic mouse models of Alzheimer’s disease. Journal of Neuroscience 28: 14392-14400.
- Ho A, Morishita W, Atasoy D, Liu X, Tabuchi K, Hammer RE, Malenka RC, Südhof TC (2006) Genetic analysis of Mint/X11 proteins: Essential presynaptic functions of a neuronal adaptor protein family. Journal of Neuroscience 26:13089-13101.
- Ho A, Südhof TC (2004) Binding of F-spondin to amyloid-beta precursor protein: a candidate amyloid beta precursor protein ligand that modulates amyloid-beta precursor protein cleavage. Proceedings of the National Academy Sciences 101:2549-2553.